Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1985 Dec 1;232(2):617–620. doi: 10.1042/bj2320617

13C-n.m.r. study of C hordein.

A S Tatham, P R Shewry, P S Belton
PMCID: PMC1152925  PMID: 4091813

Abstract

The structure of C hordein was studied by a combination of solution and solid-state 13C-n.m.r. spectroscopy. The repetitive primary structure results in simple solution-state n.m.r. spectra, which allow assignment of the majority of the resonances to five major residues. The major resonances, with the exception of the aromatic signals, are also present in the solid-state spectra. The proline residues are in the trans configuration, consistent with an earlier study suggesting a beta-turn-rich structure.

Full text

PDF
617

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Forde B. G., Kreis M., Williamson M. S., Fry R. P., Pywell J., Shewry P. R., Bunce N., Miflin B. J. Short tandem repeats shared by B- and C-hordein cDNAs suggest a common evolutionary origin for two groups of cereal storage protein genes. EMBO J. 1985 Jan;4(1):9–15. doi: 10.1002/j.1460-2075.1985.tb02310.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Tatham A. S., Drake A. F., Shewry P. R. A conformational study of a glutamine- and proline-rich cereal seed protein, C hordein. Biochem J. 1985 Mar 1;226(2):557–562. doi: 10.1042/bj2260557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Urry D. W. Characterization of soluble peptides of elastin by physical techniques. Methods Enzymol. 1982;82(Pt A):673–716. doi: 10.1016/0076-6879(82)82096-x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES